Available applications

Background of GRAP2 antibody

In general, it exists in association with catalytic domains, as in the nonreceptor protein-tyrosine kinases and phospholipase C-γ, within structural proteins, such as spectrin or myosin, and in small adapter proteins, such as Crk and GRB2. SH3 domains are often accompanied by SH2 domains of 100 amino acids that bind to tyrosine-phosphorylated regions of target proteins, frequently linking activated growth factors to putative signal transduction proteins. Deletion or mutation of SH3 domains generally activates the transforming potential of nonreceptor tyrosine kinases, suggesting that SH3 mediates negative regulation of an intrinsic transforming activity. Gads is an adapter proteins that contains both SH2 and SH3 domains. Gads binds to tyrosine-phosphorylated proteins, such as Shc, and functions to couple these proteins to downstream effectors.

HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY GRAP2 (RC206546, Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-GRAP2.